Evidence map›Paper›PMID 28956068›Full record

ArticleCellular and molecular life sciences : CMLS2018

Amyloid precursor protein products concentrate in a subset of exosomes specifically endocytosed by neurons.

Karine Laulagnier, Charlotte Javalet, Fiona J Hemming, Mathilde Chivet, Gaëlle Lachenal, Béatrice Blot, Christine Chatellard, Rémy Sadoul

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

101 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
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  6. Loading of therapeutic cell penetrating peptides into extracellular vesicles for pulmonary fibrosis.Journal of controlled release : official journal of the Controlled Release Society · 2026
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  13. Neuronal Deletion ofBiomolecules · 2025
    Article
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41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Karine LaulagnierInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France. klaulagn@gmail.com.
Charlotte JavaletInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France.
Fiona J HemmingInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France.
Mathilde ChivetDulbecco Telethon Institute Lab of Neurodegenerative Diseases, Centre for Integrative Biology (CIBIO), University of Trento, 38123, Trento, Italy.
Gaëlle LachenalInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France.
Béatrice BlotInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France.
Christine ChatellardInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France.
Rémy SadoulInstitut National de la Santé et de la Recherche Médicale (INSERM), U1216, 38042, Grenoble, France. remy.sadoul@univ-grenoble-alpes.fr.
Inserm · FRDulbecco Telethon Institute · ITGrenoble Institute of Neurosciences · FRUniversité Grenoble Alpes · FR

Funding

Agence Nationale de la Recherche MALZ
6 · The paper itself

Abstract

Amyloid beta peptide (Aβ), the main component of senile plaques of Alzheimer's disease brains, is produced by sequential cleavage of amyloid precursor protein (APP) and of its C-terminal fragments (CTFs). An unanswered question is how amyloidogenic peptides spread throughout the brain during the course of the disease. Here, we show that small lipid vesicles called exosomes, secreted in the extracellular milieu by cortical neurons, carry endogenous APP and are strikingly enriched in CTF-α and the newly characterized CTF-η. Exosomes from N2a cells expressing human APP with the autosomal dominant Swedish mutation contain Aβ peptides as well as CTF-α and CTF-η, while those from cells expressing the non-mutated form of APP only contain CTF-α and CTF-η. APP and CTFs are sorted into a subset of exosomes which lack the tetraspanin CD63 and specifically bind to dendrites of neurons, unlike exosomes carrying CD63 which bind to both neurons and glial cells. Thus, neuroblastoma cells secrete distinct populations of exosomes carrying different cargoes and targeting specific cell types. APP-carrying exosomes can be endocytosed by receiving cells, allowing the processing of APP acquired by exosomes to give rise to the APP intracellular domain (AICD). Thus, our results show for the first time that neuronal exosomes may indeed act as vehicles for the intercellular transport of APP and its catabolites.

Indexed as

EndocytosisAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsBrainCells, CulturedEmbryo, MammalianExosomesFemaleHumansNeuronsPlaque, AmyloidPregnancyProtein TransportRatsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorCTF-C83CTF-C99Extracellular vesiclesIntercellular communicationNeurodegenerative disorders

Identifiers

PMID28956068
PMCPMC11105273
OpenAlexW2759574006

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.